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A Non-Active Site Residue, Cysteine 69, Of Glutathione S-Transferase Adgstd3-3 Has A Role In Stability And Catalytic Function.

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Abstract:

The Cys69 residue of an Anopheles dirus glutathione S-transferase isoform (adGSTD3-3), was characterized to elucidate its contribution in both catalysis and structural support. Nine mutants were generated at this position by replacing the residue with polar, non-polar and charged residues. The polar residues changed the Vm of the enzymes. With non-polar residues, the enzymes were unable to fold and were expressed in the insoluble inclusion form. With charged residues, the soluble enzyme yields were only 3% of the wild type protein. Molecular dynamics simulation also was performed to understand the changes in the enzyme structure. These findings are additional evidence of the importance of structural residues that affect the enzymatic properties such as Vm, Km and enzyme specificity.

Keywords: anopheles dirus; catalysis; glutathione transferase; mosquito; mutagenesis

Document Type: Review Article

DOI: https://doi.org/10.2174/0929866033478870

Affiliations: Institute of Molecular Biology and Genetics, Mahidol University Salaya Campus, Salaya, Nakhon Pathom 73170, Thailand

Publication date: 2003-08-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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